Conformation and processing of cathepsin D View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

1985-10

AUTHORS

Roger H. Pain, Tamara Lan, Vito Turk

ABSTRACT

Cathepsin D occurs in two forms, a single polypeptide chain (Mr 44 000) and a non-covalent complex of two peptides of Mr 14 000 and 30 000 that is derived by proteolytic processing of the 44 000 polypeptide. The two forms from bovine spleen are closely similar in secondary structure content, in aromatic amino acid environment and in the two step denaturation behaviour. Enzyme activity is lost irreversibly on denaturation but conformation can be partially regained. The two separated chains will only refold partially and this is related to their positions in the overall structure of cathepsin D. It is suggested that the processing step is related to protein turnover. More... »

PAGES

957-967

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf01119908

DOI

http://dx.doi.org/10.1007/bf01119908

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1048837076

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/3830270


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